TTLL9_BOVIN
ID TTLL9_BOVIN Reviewed; 461 AA.
AC Q3SZH6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable tubulin polyglutamylase TTLL9 {ECO:0000250|UniProtKB:A2APC3};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:A2APC3};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 9;
GN Name=TTLL9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable tubulin polyglutamylase that generates side chains
CC of glutamate on the gamma-carboxyl group of specific glutamate residues
CC within the C-terminal tail of target proteins. Similar to TTLL1, may
CC acquire enzymatic activity only in complex with other proteins as it is
CC most likely lacking domains important for autonomous activity. Mediates
CC tubulin polyglutamylation which induces establishment of microtubule
CC heterogeneity in sperm flagella, thereby playing a role in normal
CC motile flagella axoneme structure and sperm flagella beating pattern.
CC {ECO:0000250|UniProtKB:A2APC3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP +
CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein]
CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519,
CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:A2APC3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149;
CC Evidence={ECO:0000250|UniProtKB:A2APC3};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:A2APC3}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:A2APC3}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:A2APC3}.
CC -!- DOMAIN: Gln-155 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
CC -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC {ECO:0000305}.
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DR EMBL; BC102853; AAI02854.1; -; mRNA.
DR RefSeq; NP_001030455.1; NM_001035378.2.
DR AlphaFoldDB; Q3SZH6; -.
DR SMR; Q3SZH6; -.
DR STRING; 9913.ENSBTAP00000012842; -.
DR PaxDb; Q3SZH6; -.
DR Ensembl; ENSBTAT00000082103; ENSBTAP00000058899; ENSBTAG00000005937.
DR GeneID; 529246; -.
DR KEGG; bta:529246; -.
DR CTD; 164395; -.
DR VEuPathDB; HostDB:ENSBTAG00000005937; -.
DR VGNC; VGNC:36496; TTLL9.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000159879; -.
DR HOGENOM; CLU_010131_0_1_1; -.
DR InParanoid; Q3SZH6; -.
DR OMA; LIWANGP; -.
DR OrthoDB; 584228at2759; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000005937; Expressed in semen and 79 other tissues.
DR ExpressionAtlas; Q3SZH6; baseline.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; ISS:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018095; P:protein polyglutamylation; IBA:GO_Central.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027751; TTLL9.
DR PANTHER; PTHR12241:SF39; PTHR12241:SF39; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Cilium; Cytoplasm; Cytoskeleton; Flagellum;
KW Ligase; Magnesium; Metal-binding; Microtubule; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..461
FT /note="Probable tubulin polyglutamylase TTLL9"
FT /id="PRO_0000324516"
FT DOMAIN 22..402
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..279
FT /note="L-glutamate"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT COMPBIAS 184..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 155..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 155
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 218..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 231..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 257
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 276..277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 294
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 363
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 379
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 155
FT /note="Essential for specifying alpha-elongation versus
FT initiation step of the polyglutamylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
SQ SEQUENCE 461 AA; 54111 MW; 690D5290E5F2D6D5 CRC64;
MSRPKNQNYK GHGLQKGKER EQRASIRFKT TLMNTLMDVL RHRPGWVEVK DEGEWDFYWC
DVSWLRENFD HTYMGEHVRI SHFRNHYELT RKNYMVKNLK RFRKQLEREA GKLEAAKCDF
FPKTFEMPCE YHLFVEEFRK NPGITWIMKP VARSQGKGIF LFRRLKDIMD WKKGTAGKKL
TSLEAQPARN TVNPSGSHDT RSSDDQKDEI PVENYVAQRY IENPYLIGGR KFDLRVYVLV
MSYIPLRAWL YRDGFARFSN TRFTLNSIDD QYVHLTNVAV QKTSPDYHPK KGCKWMLQRF
RQYLASKHGP EAVETLFSDM DNIFIRSLQS VQKVIISDKH CFELYGYDIL IDQDLKPWLL
EVNASPSLTA SSQEDYELKT CLLEDTLHIV DMEARLTGRE KRVGGFDLMW NDGPVSREEG
GPDLSGMGNF VTNTHLGCVN DRKEQLRQLF RSLQGQKKTP N
